Evidence map›Paper›PMID 32661420›Full record

ArticleNature structural & molecular biology2020

Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism.

Byung-Gil Lee, Fabian Merkel, Matteo Allegretti, Markus Hassler, Christopher Cawood, Léa Lecomte, Francis J O'Reilly, Ludwig R Sinn, Pilar Gutierrez-Escribano, Marc Kschonsak and 7 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

68 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Gel Electrophoresis Analysis of SMC-Mediated Effects on DNA Topology.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  10. Article
  11. Condensin-Condensin Interactions Facilitate Mitotic Chromosome Assembly in Xenopus Egg Extracts.Genes to cells : devoted to molecular & cellular mechanisms · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Mitotic genome folding.The Journal of cell biology · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

8 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

17 authors.

Byung-Gil Lee *MRC Laboratory of Molecular Biology, Cambridge, UK.
Fabian Merkel *Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0002-7477-5699
Matteo AllegrettiStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0002-9542-7482
Markus HasslerCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0001-9827-3477
Christopher CawoodMRC London Institute of Medical Sciences, London, UK.ORCID http://orcid.org/0000-0001-7419-5419
Léa LecomteCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0002-1149-7230
Francis J O'ReillyInstitute of Biotechnology, Technische Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0001-9258-0150
Ludwig R SinnInstitute of Biotechnology, Technische Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0003-4692-0681
Pilar Gutierrez-EscribanoMRC London Institute of Medical Sciences, London, UK.
Marc KschonsakCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Sol BravoCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0001-9007-5169
Takanori NakaneMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0003-2697-2767
Juri RappsilberInstitute of Biotechnology, Technische Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0001-5999-1310
Luis AragonMRC London Institute of Medical Sciences, London, UK. luis.aragon@lms.mrc.ac.uk.ORCID http://orcid.org/0000-0003-0634-6742
Martin BeckCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany. martin.beck@embl.de.ORCID http://orcid.org/0000-0002-7397-1321
Jan LöweMRC Laboratory of Molecular Biology, Cambridge, UK. jyl@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0002-5218-6615
Christian H HaeringCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany. christian.haering@uni-wuerzburg.de.ORCID http://orcid.org/0000-0001-8301-1722

Funding

Medical Research Council MC-A652-5PY00Medical Research Council MC_U105184326Medical Research Council MC_U120074328Medical Research Council U105184326Wellcome Trust 100955Wellcome Trust 100955/Z/13/ZWellcome Trust 202754Wellcome Trust 202754/Z/16/Z
6 · The paper itself

Abstract

Complexes containing a pair of structural maintenance of chromosomes (SMC) family proteins are fundamental for the three-dimensional (3D) organization of genomes in all domains of life. The eukaryotic SMC complexes cohesin and condensin are thought to fold interphase and mitotic chromosomes, respectively, into large loop domains, although the underlying molecular mechanisms have remained unknown. We used cryo-EM to investigate the nucleotide-driven reaction cycle of condensin from the budding yeast Saccharomyces cerevisiae. Our structures of the five-subunit condensin holo complex at different functional stages suggest that ATP binding induces the transition of the SMC coiled coils from a folded-rod conformation into a more open architecture. ATP binding simultaneously triggers the exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains. We propose that these steps result in the interconversion of DNA-binding sites in the catalytic core of condensin, forming the basis of the DNA translocation and loop-extrusion activities.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateCarrier ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCryoelectron MicroscopyDNA-Binding ProteinsModels, MolecularMultiprotein ComplexesNuclear ProteinsProtein ConformationProtein FoldingProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesAdenosine TriphosphateCarrier ProteinsCell Cycle ProteinsChromosomal Proteins, Non-Histonecondensin complexesDNA-Binding ProteinsMultiprotein ComplexesNuclear ProteinsSaccharomyces cerevisiae ProteinsSMC2 protein, S cerevisiaeSMC4 protein, S cerevisiae

Identifiers

PMID32661420
PMCPMC7610691

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.